Reviewed, UniProtKB/Swiss-Prot Q01159 (MCE1_YEAST)

Names and origin

Protein names

Recommended name:
    mRNA-capping enzyme subunit alpha
Alternative name(s):
    mRNA guanylyltransferase
    EC=2.7.7.50
    GTP--RNA guanylyltransferase
      Short name=GTase

Gene names

Name:	CEG1
Ordered Locus Names:	YGL130W
ORF Names:	G2853

Organism

Saccharomyces cerevisiae (Baker's yeast) [Complete proteome]

Taxonomic identifier

4932 [NCBI]

Taxonomic lineage

Eukaryota › Fungi › Dikarya › Ascomycota › Saccharomycotina › Saccharomycetes › Saccharomycetales › Saccharomycetaceae › Saccharomyces

Protein attributes

Sequence length	459 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Second step of mRNA capping. Transfer of the GMP moiety of GTP to the 5'-end of RNA via an enzyme-GMP covalent reaction intermediate.
Catalytic activity	GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA.
Cofactor	Divalent ions.
Subunit structure	The mRNA-capping enzyme is composed of two separate chains alpha and beta, respectively a mRNA guanylyltransferase and an RNA 5'-triphosphatase.
Subcellular location	Nucleus.
Miscellaneous	Present with 279 molecules/cell in log phase SD medium. Ref.11
Sequence similarities	Belongs to the eukaryotic GTase family.

Ontologies

Keywords
Biological process	mRNA capping mRNA processing
Cellular component	Nucleus
Ligand	GTP-binding Nucleotide-binding
Molecular function	Nucleotidyltransferase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	mRNA capping Inferred from mutant phenotype. Source: SGD positive regulation of transcription from RNA polymerase II promoter Inferred from genetic interaction. Source: SGD
Cellular component	mRNA capping enzyme complex Inferred from genetic interaction. Source: SGD
Molecular function	GTP binding Inferred from electronic annotation. Source: UniProtKB-KW mRNA guanylyltransferase activity Inferred from mutant phenotype. Source: SGD protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CET1	O13297	1	EBI-10503,EBI-4473

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 459	459	mRNA-capping enzyme subunit alpha		PRO_0000210106
Sites
	Active site	70	1	N6-GMP-lysine intermediate Ref.7
Experimental info
	Mutagenesis	57	1	E → A: No effect.
	Mutagenesis	58	1	E → A: No effect.
	Mutagenesis	59	1	K → A, T, S or R: No effect. Ref.7
	Mutagenesis	66	1	Y → A: Temperature-sensitive.
	Mutagenesis	70	1	K → A, R, M, I or T: Lethal. Ref.7
	Mutagenesis	71	1	T → A: No effect.
	Mutagenesis	72	1	D → A: No effect.
	Mutagenesis	73	1	G → A: Lethal.
	Mutagenesis	95	1	D → A: Temperature-sensitive.
	Mutagenesis	96	1	R → A: Temperature-sensitive.
	Mutagenesis	97	1	E → A: Temperature-sensitive.
	Mutagenesis	107 – 109	3	RFP → AAA: Reduced growth at 25 degrees and lethal at 37 degrees.
	Mutagenesis	114	1	K → A: No effect.
	Mutagenesis	115	1	K → A: No effect.
	Mutagenesis	116	1	K → A: No effect.
	Mutagenesis	117	1	E → A: No effect.
	Mutagenesis	118	1	E → A: No effect.
	Mutagenesis	129	1	L → A: No effect.
	Mutagenesis	130	1	D → A: Lethal.
	Mutagenesis	131	1	G → A: Temperature-sensitive.
	Mutagenesis	132	1	E → A: Lethal.
	Mutagenesis	134	1	V → A: No effect.
	Mutagenesis	218	1	D → A: No effect.
	Mutagenesis	219	1	K → A: No effect.
	Mutagenesis	225	1	D → A: Lethal.
	Mutagenesis	226	1	G → A: Lethal.
	Mutagenesis	241	1	K → A: No effect.
	Mutagenesis	242	1	D → A: No effect.
	Mutagenesis	249	1	K → A: Lethal.
	Mutagenesis	253	1	E → A: No effect.
	Mutagenesis	254	1	N → A: No effect.
	Mutagenesis	255	1	T → A: Temperature-sensitive.
	Mutagenesis	257	1	D → A: Lethal.
	Mutagenesis	274	1	K → A: No effect.
	Mutagenesis	275	1	D → A: No effect.
	Mutagenesis	276	1	D → A: No effect.
	Mutagenesis	395	1	E → A: No effect.
	Mutagenesis	396	1	D → A: No effect.
	Sequence conflict	45	1	G → S Ref.3
	Sequence conflict	300	1	D → N Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Q01159-1 [UniParc]. Last modified February 1, 1995. Version 2. Checksum: F7F5A3E59EEFA15F	FASTA	459	52,764
	10 20 30 40 50 60 MVLAMESRVA PEIPGLIQPG NVTQDLKMMV CKLLNSPKPT KTFPGSQPVS FQHSDVEEKL 70 80 90 100 110 120 LAHDYYVCEK TDGLRVLMFI VINPVTGEQG CFMIDRENNY YLVNGFRFPR LPQKKKEELL 130 140 150 160 170 180 ETLQDGTLLD GELVIQTNPM TKLQELRYLM FDCLAINGRC LTQSPTSSRL AHLGKEFFKP 190 200 210 220 230 240 YFDLRAAYPN RCTTFPFKIS MKHMDFSYQL VKVAKSLDKL PHLSDGLIFT PVKAPYTAGG 250 260 270 280 290 300 KDSLLLKWKP EQENTVDFKL ILDIPMVEDP SLPKDDRNRW YYNYDVKPVF SLYVWQGGAD 310 320 330 340 350 360 VNSRLKHFDQ PFDRKEFEIL ERTYRKFAEL SVSDEEWQNL KNLEQPLNGR IVECAKNQET 370 380 390 400 410 420 GAWEMLRFRD DKLNGNHTSV VQKVLESIND SVSLEDLEEI VGDIKRCWDE RRANMAGGSG 430 440 450 RPLPSQSQNA TLSTSKPVHS QPPSNDKEPK YVDEDDWSD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"mRNA capping enzyme. Isolation and characterization of the gene encoding mRNA guanylytransferase subunit from Saccharomyces cerevisiae." Shibagaki Y., Itoh N., Yamada H., Nagata S., Mizumoto K. J. Biol. Chem. 267:9521-9528(1992) [PubMed: 1315757] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: DBY939.
[2]	Mizumoto K. Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 29-30.
[3]	"Isolation of temperature-sensitive mutants for mRNA capping enzyme in Saccharomyces cerevisiae." Yamagishi M., Mizumoto K., Ishihama A. Mol. Gen. Genet. 249:147-154(1995) [PubMed: 7500935] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Sequence analysis of a 10 kb DNA fragment from yeast chromosome VII reveals a novel member of the DnaJ family." Rodriguez-Belmonte E., Rodriguez Torres A.M., Tizon B., Cadahia J.L., Gonzalez-Siso I., Ramil E., Becerra M., Gonzalez-Dominguez M., Cerdan E. Yeast 12:145-148(1996) [PubMed: 8686378] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[5]	"The nucleotide sequence of Saccharomyces cerevisiae chromosome VII." Tettelin H., Agostoni-Carbone M.L., Albermann K., Albers M., Arroyo J., Backes U., Barreiros T., Bertani I., Bjourson A.J., Brueckner M., Bruschi C.V., Carignani G., Castagnoli L., Cerdan E., Clemente M.L., Coblenz A., Coglievina M., Coissac E. , Defoor E., Del Bino S., Delius H., Delneri D., de Wergifosse P., Dujon B., Durand P., Entian K.-D., Eraso P., Escribano V., Fabiani L., Fartmann B., Feroli F., Feuermann M., Frontali L., Garcia-Gonzalez M., Garcia-Saez M.I., Goffeau A., Guerreiro P., Hani J., Hansen M., Hebling U., Hernandez K., Heumann K., Hilger F., Hofmann B., Indge K.J., James C.M., Klima R., Koetter P., Kramer B., Kramer W., Lauquin G., Leuther H., Louis E.J., Maillier E., Marconi A., Martegani E., Mazon M.J., Mazzoni C., McReynolds A.D.K., Melchioretto P., Mewes H.-W., Minenkova O., Mueller-Auer S., Nawrocki A., Netter P., Neu R., Nombela C., Oliver S.G., Panzeri L., Paoluzi S., Plevani P., Portetelle D., Portillo F., Potier S., Purnelle B., Rieger M., Riles L., Rinaldi T., Robben J., Rodrigues-Pousada C., Rodriguez-Belmonte E., Rodriguez-Torres A.M., Rose M., Ruzzi M., Saliola M., Sanchez-Perez M., Schaefer B., Schaefer M., Scharfe M., Schmidheini T., Schreer A., Skala J., Souciet J.-L., Steensma H.Y., Talla E., Thierry A., Vandenbol M., van der Aart Q.J.M., Van Dyck L., Vanoni M., Verhasselt P., Voet M., Volckaert G., Wambutt R., Watson M.D., Weber N., Wedler E., Wedler H., Wipfli P., Wolf K., Wright L.F., Zaccaria P., Zimmermann M., Zollner A., Kleine K. Nature 387:81-84(1997) [PubMed: 9169869] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 96604 / S288c / FY1679.
[6]	"Covalent catalysis in nucleotidyl transfer reactions: essential motifs in Saccharomyces cerevisiae RNA capping enzyme are conserved in Schizosaccharomyces pombe and viral capping enzymes and among polynucleotide ligases." Shuman S., Liu Y., Schwer B. Proc. Natl. Acad. Sci. U.S.A. 91:12046-12050(1994) [PubMed: 7991582] [Abstract] Cited for: MUTAGENESIS.
[7]	"Active site of the mRNA-capping enzyme guanylyltransferase from Saccharomyces cerevisiae: similarity to the nucleotidyl attachment motif of DNA and RNA ligases." Fresco L.D., Buratowski S. Proc. Natl. Acad. Sci. U.S.A. 91:6624-6628(1994) [PubMed: 8022828] [Abstract] Cited for: ACTIVE SITE, MUTAGENESIS OF LYS-59 AND LYS-70.
[8]	"Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. I. Purification and subunit structure." Itoh N., Mizumoto K., Kaziro Y. J. Biol. Chem. 259:13923-13929(1984) [PubMed: 6389537] [Abstract] Cited for: CHARACTERIZATION.
[9]	"Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. II. Catalytic properties." Itoh N., Mizumoto K., Kaziro Y. J. Biol. Chem. 259:13930-13936(1984) [PubMed: 6094533] [Abstract] Cited for: CHARACTERIZATION.
[10]	"Messenger RNA guanylyltransferase from Saccharomyces cerevisiae. Large scale purification, subunit functions, and subcellular localization." Itoh N., Yamada H., Kaziro Y., Mizumoto K. J. Biol. Chem. 262:1989-1995(1987) [PubMed: 3029058] [Abstract] Cited for: CHARACTERIZATION.
[11]	"Global analysis of protein expression in yeast." Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S. Nature 425:737-741(2003) [PubMed: 14562106] [Abstract] Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	D10263 Genomic DNA. Translation: BAA01103.1. X87252 Genomic DNA. Translation: CAA60705.1. Z72652 Genomic DNA. Translation: CAA96839.1.
PIR	S59731.
RefSeq	NP_011385.1.
3D structure databases
HSSP	HSSP built from PDB template 1P16 based on UniProtKB P78587.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP:2298N.
IntAct	Q01159. 29 interactions.
Proteomic databases
PeptideAtlas	Q01159.
PRIDE	Q01159.
Genome annotation databases
Ensembl	YGL130W. Saccharomyces cerevisiae. [Contig view]
GeneID	852747.
GenomeReviews	Gene locus YGL130W in contig Y13135_GR.
KEGG	sce:YGL130W.
NMPDR	fig|4932.3.peg.2489.
Organism-specific databases
CYGD	YGL130w.
SGD	S000003098. CEG1.
Yeast-GFP	Search...
Phylogenomic databases
HOGENOM	Q01159.
OMA	Q01159. DGLIFTC.
Enzyme and pathway databases
BRENDA	2.7.7.50. 250.
Gene expression databases
ArrayExpress	Q01159.
GermOnline	YGL130W. Saccharomyces cerevisiae.
Family and domain databases
InterPro	IPR001339. mRNA_cap_enzyme. IPR013846. mRNA_cap_enzyme_C. IPR017075. mRNA_capping_enz_asu. IPR012340. NA-bd_OB-fold. [Graphical view]
Gene3D	G3DSA:2.40.50.140. OB_NA_bd_sub. 1 hit.
Pfam	PF03919. mRNA_cap_C. 1 hit. PF01331. mRNA_cap_enzyme. 1 hit. [Graphical view]
PIRSF	PIRSF036959. mRNA_cap_alpha. 1 hit.
ProtoNet	Search...
Other Resources
NextBio	972171.

Entry information

Entry name

MCE1_YEAST

Accession

Primary (citable) accession number: Q01159
Secondary accession number(s): Q9URD1

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1993
Last sequence update:	February 1, 1995
Last modified:	June 16, 2009
This is version 88 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

FPAP (Fungal Proteome Annotation Project)